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S52A3_AILME
ID   S52A3_AILME             Reviewed;         469 AA.
AC   D2HSA6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Solute carrier family 52, riboflavin transporter, member 3;
DE   AltName: Full=Riboflavin transporter 2;
DE            Short=RFT2;
GN   Name=SLC52A3; Synonyms=RFT2; ORFNames=PANDA_014962;
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA   Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA   Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA   Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA   Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA   Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA   Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA   Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA   Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA   Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA   Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA   Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA   Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA   Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA   Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
CC   -!- FUNCTION: Plasma membrane transporter mediating the uptake by cells of
CC       the water soluble vitamin B2/riboflavin that plays a key role in
CC       biochemical oxidation-reduction reactions of the carbohydrate, lipid,
CC       and amino acid metabolism. {ECO:0000250|UniProtKB:Q9NQ40}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC         ChEBI:CHEBI:57986; Evidence={ECO:0000250|UniProtKB:Q9NQ40};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NQ40};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the riboflavin transporter family.
CC       {ECO:0000305}.
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DR   EMBL; GL193270; EFB29584.1; -; Genomic_DNA.
DR   RefSeq; XP_002925444.1; XM_002925398.3.
DR   RefSeq; XP_019661681.1; XM_019806122.1.
DR   RefSeq; XP_019661682.1; XM_019806123.1.
DR   RefSeq; XP_019661683.1; XM_019806124.1.
DR   RefSeq; XP_019661684.1; XM_019806125.1.
DR   RefSeq; XP_019661685.1; XM_019806126.1.
DR   RefSeq; XP_019661686.1; XM_019806127.1.
DR   AlphaFoldDB; D2HSA6; -.
DR   STRING; 9646.ENSAMEP00000014844; -.
DR   GeneID; 100472037; -.
DR   CTD; 113278; -.
DR   eggNOG; KOG4255; Eukaryota.
DR   InParanoid; D2HSA6; -.
DR   OrthoDB; 757564at2759; -.
DR   Proteomes; UP000008912; Unassembled WGS sequence.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0032218; P:riboflavin transport; ISS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
DR   InterPro; IPR009357; Riboflavin_transptr.
DR   PANTHER; PTHR12929; PTHR12929; 1.
DR   Pfam; PF06237; DUF1011; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..469
FT                   /note="Solute carrier family 52, riboflavin transporter,
FT                   member 3"
FT                   /id="PRO_0000399790"
FT   TOPO_DOM        1..6
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..43
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..71
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        106..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..335
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        336..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357..361
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        362..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        383..396
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        418..427
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        449..469
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          266..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q4FZU9"
FT   CARBOHYD        94
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   469 AA;  50502 MW;  9B2F8F3337AE2CF7 CRC64;
     MALLTHLLVC TFGMGSWVAI NGLWVELPLL VTELPEGWYL PSYLTMVIQL ANIGPLLVTL
     LHHFQPSCLS EVPIIFTVLA VGTVACALFA FLWNVTSWVL DGRHSIAFMV LTFFLALVDC
     TSSVTFLPFM SRLPACYLTT FFVGEGLSSL LPALVALAQG SGLTTCVNVT QPPDTTPSTA
     TTGKTVFLQG ANSTLGTDLT GTTRSAIHLE SRYLPANFSP LVFFLLLSFM MACCLAAFFL
     LQRQPRPRES SIEDLLTSQV TLHSIRPREG DDLGPPDPGP SSKAQGLPEE KTASDHPAHL
     AFIYVLVAFV NALTNGVLPS VQTYSCLSYG PVAYHLSATL SSMANPLACF LSMFLPHRSL
     PFLGVLTVLG TGFGAYNMAM AVMSPCPLMQ GHWAGEILIV ASWVLFIGCL SYVKVMLGVI
     LRDRSRSALV WCGAAVQLGS LLGALLMFPL VNVLRLFSSA DFCSLQCSA
 
 
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